Limited proteolysis of actin by a specific bacterial protease
- 8 February 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 228 (1) , 172-174
- https://doi.org/10.1016/0014-5793(88)80610-0
Abstract
A 36 kDa fragment of rabbit skeletal muscle actin resistant to further proteolytic breakdown was obtained with a new bacterial protease. This fragment was the only cleavage product obtained from native actin whereas proteolysis of heat-inactivated actin was unlimited. The 36 kDa fragment failed to polymerize and to inhibit DNase I activity. Binding to DNase I protects actin against proteolysis by protease. The results on actin proteolysis by different proteases are comparedKeywords
This publication has 7 references indexed in Scilit:
- Polymerization of β-like actin from scallop adductor muscleFEBS Letters, 1986
- Effects of various amino acid replacements on the conformational stability of G‐actinEuropean Journal of Biochemistry, 1985
- Proteolysis and structure of skeletal muscle actin.Proceedings of the National Academy of Sciences, 1984
- Studies on the antigenic sites of actin: a comparative study of the immunogenic crossreactivity of invertebrate actinsJournal of Muscle Research and Cell Motility, 1983
- Protection of actin against proteolysis by complex formation with deoxyribonuclease ICanadian Journal of Biochemistry, 1980
- ATP binding to a protease-resistant core of actin.Proceedings of the National Academy of Sciences, 1976
- Actin Is the Naturally Occurring Inhibitor of Deoxyribonuclease IProceedings of the National Academy of Sciences, 1974